title: Temperature and the catalytic activity of enzymes: a fresh understanding.
abstract: The discovery of an additional step in the progression of an enzyme from the active to inactive state under the influence of temperature has led to a better match with experimental data for all enzymes that follow Michaelis-Menten kinetics, and to an increased understanding of the process. The new model of the process, the Equilibrium Model, describes an additional mechanism by which temperature affects the activity of enzymes, with implications for ecological, metabolic, structural, and applied studies of enzymes.
authors.affiliation: Thermophile Research Unit, Department of Biological Sciences, University of Waikato, Hamilton, New Zealand.
authors.forename: Roy M
authors.initials: RM
authors.lastname: Daniel
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Danson
mesh_terms: D000465:Algorithms; D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D013696:Temperature
chemical_list: D004798:Enzymes
keywords: Catalytic activity; Enzyme; Equilibrium Model; Temperature